1. Field of the Invention
The present invention relates to the field of immunology. More specifically, the present invention relates to canine immunoglobulin light and heavy chain variable domains, caninized antibodies, and methods for making and using them.
2. Summary of the Related Art
The process of modifying a monoclonal antibody from an animal to render it less immunogenic for therapeutic administration to humans (humanization) has been aggressively pursued and has been described in a number of publications (e.g. Antibody Engineering: A practical Guide. Carl A. K. Borrebaeck ed. W.H. Freeman and Company, 1992). However, this process has not been applied for the development of therapeutic or diagnostics for canines. In fact, very little has been published with regard to canine variable domains at all.
Wasserman and Capra, Biochem. 16, 3160 (1977), determined the amino acid sequence of the variable regions of both a canine IgM and a canine IgA heavy chain.
Wasserman and Capra, Immunochem. 15, 303 (1978), determined the amino acid sequence of the κ light chain from a canine IgA.
McCumber and Capra, Mol. Immunol. 16, 565 (1979), disclose the complete amino-acid sequence of a canine mu chain.
Tang et al., Vet. Immunology Immunopathology 80, 259 (2001), discloses a single canine IgG-A γ chain cDNA and four canine IgG-A γ chain protein sequences. It describes PCR amplification of a canine spleen cDNA library with a degenerate oligonucleotide primer designed from the conserved regions of human, mouse, pig, and bovine IgGs.
The paucity of information available on canine antibodies prevents their development as therapeutics for the treatment canine disease.
All publications recited in this specification (e.g., patent publications and scientific journal articles) are hereby incorporated by reference in their entirety.